ArticleThe Journal of biological chemistry2014
Concerted all-or-none subunit interactions mediate slow deactivation of human ether-à-go-go-related gene K+ channels.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed.
- Determinants of Isoform-Specific Gating Kinetics of hERG1 Channel: Combined Experimental and Simulation Study.Frontiers in physiology · 2018Article
- Rescue of protein expression defects may not be enough to abolish the pro-arrhythmic phenotype of long QT type 2 mutations.The Journal of physiology · 2016Article
- Molecular Basis of Cardiac Delayed Rectifier Potassium Channel Function and Pharmacology.Cardiac electrophysiology clinics · 2016Review
- Intersubunit Concerted Cooperative and cis-Type Mechanisms Modulate Allosteric Gating in Two-Pore-Domain Potassium Channel TREK-2.Frontiers in cellular neuroscience · 2016Article
- An Interdomain KCNH2 Mutation Produces an Intermediate Long QT Syndrome.Human mutation · 2015Article
- C-Linker Accounts for Differential Sensitivity of ERG1 and ERG2 K+ Channels to RPR260243-Induced Slow Deactivation.Molecular pharmacology · 2015Article
- Getting to the heart of hERG K(+) channel gating.The Journal of physiology · 2015Review
- Identification of the Intracellular Na+ Sensor in Slo2.1 Potassium Channels.The Journal of biological chemistry · 2015Article
- Sequence of gating charge movement and pore gating in HERG activation and deactivation pathways.Biophysical journal · 2015Article
- Concatenated hERG1 tetramers reveal stoichiometry of altered channel gating by RPR-260243.Molecular pharmacology · 2015Article
Corrections and comments
- Retraction · 2016-10-07Error in Image ·
- Retracted
Authors and funding
3 authors.
Funding
Abstract
During the repolarization phase of a cardiac action potential, hERG1 K(+) channels rapidly recover from an inactivated state then slowly deactivate to a closed state. The resulting resurgence of outward current terminates the plateau phase and is thus a key regulator of action potential duration of cardiomyocytes. The intracellular N-terminal domain of the hERG1 subunit is required for slow deactivation of the channel as its removal accelerates deactivation 10-fold. Here we investigate the stoichiometry of hERG1 channel deactivation by characterizing the kinetic properties of concatenated tetramers containing a variable number of wild-type and mutant subunits. Three mutations known to accelerate deactivation were investigated, including R56Q and R4A/R5A in the N terminus and F656I in the S6 transmembrane segment. In all cases, a single mutant subunit induced the same rapid deactivation of a concatenated channel as that observed for homotetrameric mutant channels. We conclude that slow deactivation gating of hERG1 channels involves a concerted, fully cooperative interaction between all four wild-type channel subunits.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.